+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 7upn | ||||||
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タイトル | Maedi visna virus Vif in complex with CypA and E3 ubiquitin ligase | ||||||
要素 |
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キーワード | ISOMERASE/VIRAL PROTEIN / virus-host interacting complex / ISOMERASE-VIRAL PROTEIN complex | ||||||
機能・相同性 | 機能・相同性情報 negative regulation of protein K48-linked ubiquitination / negative regulation of viral life cycle / regulation of apoptotic signaling pathway / cell adhesion molecule production / lipid droplet organization / target-directed miRNA degradation / elongin complex / heparan sulfate binding / regulation of viral genome replication / VCB complex ...negative regulation of protein K48-linked ubiquitination / negative regulation of viral life cycle / regulation of apoptotic signaling pathway / cell adhesion molecule production / lipid droplet organization / target-directed miRNA degradation / elongin complex / heparan sulfate binding / regulation of viral genome replication / VCB complex / leukocyte chemotaxis / negative regulation of stress-activated MAPK cascade / endothelial cell activation / virion binding / Basigin interactions / Cul5-RING ubiquitin ligase complex / Cul2-RING ubiquitin ligase complex / cyclosporin A binding / Minus-strand DNA synthesis / Plus-strand DNA synthesis / Uncoating of the HIV Virion / Early Phase of HIV Life Cycle / Integration of provirus / APOBEC3G mediated resistance to HIV-1 infection / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / Calcineurin activates NFAT / viral release from host cell / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / Binding and entry of HIV virion / positive regulation of viral genome replication / Formation of HIV elongation complex in the absence of HIV Tat / protein peptidyl-prolyl isomerization / RNA Polymerase II Transcription Elongation / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / Formation of RNA Pol II elongation complex / positive regulation of protein dephosphorylation / RNA Polymerase II Pre-transcription Events / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / activation of protein kinase B activity / 好中球 / transcription corepressor binding / negative regulation of protein phosphorylation / プロリルイソメラーゼ / Evasion by RSV of host interferon responses / virion component / peptidyl-prolyl cis-trans isomerase activity / transcription elongation by RNA polymerase II / positive regulation of protein secretion / transcription initiation at RNA polymerase II promoter / TP53 Regulates Transcription of DNA Repair Genes / Vif-mediated degradation of APOBEC3G / negative regulation of protein kinase activity / Assembly Of The HIV Virion / Budding and maturation of HIV virion / neuron differentiation / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Inactivation of CSF3 (G-CSF) signaling / 凝固・線溶系 / 血小板 / Regulation of expression of SLITs and ROBOs / SARS-CoV-1 activates/modulates innate immune responses / unfolded protein binding / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Antigen processing: Ubiquitination & Proteasome degradation / integrin binding / フォールディング / Platelet degranulation / protein-macromolecule adaptor activity / Neddylation / positive regulation of NF-kappaB transcription factor activity / cellular response to oxidative stress / ubiquitin-dependent protein catabolic process / protein-containing complex assembly / secretory granule lumen / vesicle / ficolin-1-rich granule lumen / host cell cytoplasm / positive regulation of MAPK cascade / response to hypoxia / protein ubiquitination / positive regulation of protein phosphorylation / focal adhesion / apoptotic process / ubiquitin protein ligase binding / Neutrophil degranulation / regulation of transcription by RNA polymerase II / protein-containing complex / extracellular space / RNA binding / extracellular exosome / extracellular region / 核質 / 生体膜 / 細胞核 / 細胞質基質 / 細胞質 類似検索 - 分子機能 | ||||||
生物種 | Homo sapiens (ヒト) Visna-maedi virus (ビスナウイルス) | ||||||
手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 3.5 Å | ||||||
データ登録者 | Hu, Y. / Xiong, Y. | ||||||
資金援助 | 米国, 1件
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引用 | ジャーナル: Sci Adv / 年: 2023 タイトル: Structural basis for recruitment of host CypA and E3 ubiquitin ligase by maedi-visna virus Vif. 著者: Yingxia Hu / Ragna B Gudnadóttir / Kirsten M Knecht / Fidel Arizaga / Stefán R Jónsson / Yong Xiong / 要旨: Lentiviral Vif molecules target the host antiviral APOBEC3 proteins for destruction in cellular ubiquitin-proteasome pathways. Different lentiviral Vifs have evolved to use the same canonical E3 ...Lentiviral Vif molecules target the host antiviral APOBEC3 proteins for destruction in cellular ubiquitin-proteasome pathways. Different lentiviral Vifs have evolved to use the same canonical E3 ubiquitin ligase complexes, along with distinct noncanonical host cofactors for their activities. Unlike primate lentiviral Vif, which recruits CBFβ as the noncanonical cofactor, nonprimate lentiviral Vif proteins have developed different cofactor recruitment mechanisms. Maedi-visna virus (MVV) sequesters CypA as the noncanonical cofactor for the Vif-mediated ubiquitination of ovine APOBEC3s. Here, we report the cryo-electron microscopy structure of MVV Vif in complex with CypA and E3 ligase components. The structure, along with our biochemical and functional analysis, reveals both conserved and unique structural elements of MVV Vif and its common and distinct interaction modes with various cognate cellular proteins, providing a further understanding of the evolutionary relationship between lentiviral Vifs and the molecular mechanisms by which they capture different host cofactors for immune evasion activities. | ||||||
履歴 |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 7upn.cif.gz | 204 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb7upn.ent.gz | 162.2 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 7upn.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/up/7upn ftp://data.pdbj.org/pub/pdb/validation_reports/up/7upn | HTTPS FTP |
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-関連構造データ
関連構造データ | 26673MC M: このデータのモデリングに利用したマップデータ C: 同じ文献を引用 (文献) |
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類似構造データ | 類似検索 - 機能・相同性F&H 検索 |
-リンク
-集合体
登録構造単位 |
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1 |
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-要素
#1: タンパク質 | 分子量: 18036.504 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: PPIA, CYPA / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: P62937, プロリルイソメラーゼ #2: タンパク質 | 分子量: 28182.600 Da / 分子数: 2 / 由来タイプ: 組換発現 由来: (組換発現) Visna-maedi virus (ビスナウイルス) 株: KV1772 / 遺伝子: vif / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: P69717 #3: タンパク質 | 分子量: 10843.420 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: ELOC, TCEB1 / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: Q15369 #4: タンパク質 | 分子量: 13147.781 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: ELOB, TCEB2 / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: Q15370 #5: 化合物 | 研究の焦点であるリガンドがあるか | Y | |
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-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
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EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法 |
-試料調製
構成要素 | 名称: Maedi visna virus Vif in complex with human CypA and Elongin BC components of E3 ubiquitin ligase タイプ: COMPLEX / Entity ID: #1-#4 / 由来: RECOMBINANT |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
由来(組換発現) | 生物種: Escherichia coli (大腸菌) |
緩衝液 | pH: 7.2 |
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
試料支持 | グリッドの材料: COPPER / グリッドのタイプ: C-flat-2/1 |
急速凍結 | 凍結剤: ETHANE |
-電子顕微鏡撮影
実験機器 | モデル: Titan Krios / 画像提供: FEI Company |
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顕微鏡 | モデル: FEI TITAN KRIOS |
電子銃 | 電子線源: FIELD EMISSION GUN / 加速電圧: 300 kV / 照射モード: FLOOD BEAM |
電子レンズ | モード: BRIGHT FIELDBright-field microscopy / 最大 デフォーカス(公称値): 2000 nm / 最小 デフォーカス(公称値): 900 nm |
撮影 | 電子線照射量: 62 e/Å2 / フィルム・検出器のモデル: GATAN K3 (6k x 4k) |
-解析
ソフトウェア | 名称: PHENIX / バージョン: 1.19.2_4158: / 分類: 精密化 | ||||||||||||||||||||||||
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CTF補正 | タイプ: NONE | ||||||||||||||||||||||||
対称性 | 点対称性: C2 (2回回転対称) | ||||||||||||||||||||||||
3次元再構成 | 解像度: 3.5 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 74320 / 対称性のタイプ: POINT | ||||||||||||||||||||||||
拘束条件 |
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